FA50A_HUMAN
ID FA50A_HUMAN Reviewed; 339 AA.
AC Q14320; A8KAQ4; B2R997; Q5HY37; Q6PJH5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Protein FAM50A;
DE AltName: Full=Protein HXC-26;
DE AltName: Full=Protein XAP-5;
GN Name=FAM50A; Synonyms=DXS9928E, HXC26, XAP5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=9339379; DOI=10.1006/geno.1997.4912;
RA Mazzarella R., Pengue G., Yoon J., Jones J., Schlessinger D.;
RT "Differential expression of XAP5, a candidate disease gene.";
RL Genomics 45:216-219(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 15-339.
RC TISSUE=Skeletal muscle;
RX PubMed=9039504; DOI=10.1093/dnares/3.5.337;
RA Toyoda A., Sakai T., Sugiyama Y., Kusuda J., Hashimoto K., Maeda H.;
RT "Isolation and analysis of a novel gene, HXC-26, adjacent to the rab GDP
RT dissociation inhibitor gene located at human chromosome Xq28 region.";
RL DNA Res. 3:337-340(1996).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 66-339.
RX PubMed=8733135; DOI=10.1093/hmg/5.5.659;
RA Chen E.Y., Zollo M., Mazzarella R.A., Ciccodicola A., Chen C.-N., Zuo L.,
RA Heiner C., Burough F.W., Ripetto M., Schlessinger D., D'Urso M.;
RT "Long-range sequence analysis in Xq28: thirteen known and six candidate
RT genes in 219.4 kb of high GC DNA between the RCP/GCP and G6PD loci.";
RL Hum. Mol. Genet. 5:659-668(1996).
RN [8]
RP PROTEIN SEQUENCE OF 159-170, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-100, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [12]
RP FUNCTION, INTERACTION WITH EFTUD2 AND DDX41, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, INVOLVEMENT IN MRXSA, VARIANTS MRXSA GLY-206;
RP GLY-254; ASN-255; GLY-255 AND TRP-273, CHARACTERIZATION OF VARIANTS MRXSA
RP GLY-206; GLY-254; ASN-255; GLY-255 AND TRP-273, AND CHARACTERIZATION OF
RP VARIANTS VAL-137 AND LYS-143.
RX PubMed=32703943; DOI=10.1038/s41467-020-17452-6;
RA Lee Y.R., Khan K., Armfield-Uhas K., Srikanth S., Thompson N.A., Pardo M.,
RA Yu L., Norris J.W., Peng Y., Gripp K.W., Aleck K.A., Li C., Spence E.,
RA Choi T.I., Kwon S.J., Park H.M., Yu D., Do Heo W., Mooney M.R., Baig S.M.,
RA Wentzensen I.M., Telegrafi A., McWalter K., Moreland T., Roadhouse C.,
RA Ramsey K., Lyons M.J., Skinner C., Alexov E., Katsanis N., Stevenson R.E.,
RA Choudhary J.S., Adams D.J., Kim C.H., Davis E.E., Schwartz C.E.;
RT "Mutations in FAM50A suggest that Armfield XLID syndrome is a
RT spliceosomopathy.";
RL Nat. Commun. 11:3698-3698(2020).
CC -!- FUNCTION: Probably involved in the regulation of pre-mRNA splicing.
CC {ECO:0000269|PubMed:32703943}.
CC -!- SUBUNIT: Interacts with EFTUD2, a component of the spliceosome U5
CC complex (PubMed:32703943). Interacts with DDX41, a component of the
CC spliceosome C complex (PubMed:32703943). {ECO:0000269|PubMed:32703943}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:32703943}.
CC -!- TISSUE SPECIFICITY: Widely expressed in fetal and adult tissues. Mostly
CC abundant in fetal brain, liver and kidney; in the adult, high levels
CC were also observed in heart, skeletal muscle, spleen, thymus, prostate
CC and small intestine. Expressed in fetal cerebellum and hypothalamus.
CC Low expression is observed in fetal temporal lobe (PubMed:32703943).
CC {ECO:0000269|PubMed:32703943, ECO:0000269|PubMed:9339379}.
CC -!- DISEASE: Intellectual developmental disorder, X-linked, syndromic,
CC Armfield type (MRXSA) [MIM:300261]: An X-linked recessive disorder
CC characterized by global developmental delay with impaired intellectual
CC development, walking difficulties and poor or absent speech. Affected
CC individuals display a distinctive phenotype characterized by postnatal
CC growth retardation, variable head circumference with a prominent
CC forehead and dysmorphic facial features, ocular abnormalities, and
CC seizures. {ECO:0000269|PubMed:32703943}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the FAM50 family. {ECO:0000305}.
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DR EMBL; AD001530; AAB81663.1; -; mRNA.
DR EMBL; AK293119; BAF85808.1; -; mRNA.
DR EMBL; AK313697; BAG36444.1; -; mRNA.
DR EMBL; BX936365; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471172; EAW72708.1; -; Genomic_DNA.
DR EMBL; BC000028; AAH00028.1; -; mRNA.
DR EMBL; BC015499; AAH15499.1; -; mRNA.
DR EMBL; D83389; BAA11907.1; -; Genomic_DNA.
DR EMBL; D83260; BAA11871.1; -; mRNA.
DR EMBL; L44140; AAA92649.1; -; Genomic_DNA.
DR CCDS; CCDS14751.1; -.
DR PIR; JC5276; JC5276.
DR RefSeq; NP_004690.1; NM_004699.3.
DR AlphaFoldDB; Q14320; -.
DR BioGRID; 114578; 72.
DR IntAct; Q14320; 7.
DR MINT; Q14320; -.
DR STRING; 9606.ENSP00000377225; -.
DR iPTMnet; Q14320; -.
DR MetOSite; Q14320; -.
DR PhosphoSitePlus; Q14320; -.
DR BioMuta; FAM50A; -.
DR DMDM; 12231058; -.
DR EPD; Q14320; -.
DR jPOST; Q14320; -.
DR MassIVE; Q14320; -.
DR MaxQB; Q14320; -.
DR PaxDb; Q14320; -.
DR PeptideAtlas; Q14320; -.
DR PRIDE; Q14320; -.
DR ProteomicsDB; 59964; -.
DR Antibodypedia; 488; 198 antibodies from 29 providers.
DR DNASU; 9130; -.
DR Ensembl; ENST00000393600.8; ENSP00000377225.3; ENSG00000071859.15.
DR GeneID; 9130; -.
DR KEGG; hsa:9130; -.
DR MANE-Select; ENST00000393600.8; ENSP00000377225.3; NM_004699.4; NP_004690.1.
DR UCSC; uc004fll.4; human.
DR CTD; 9130; -.
DR DisGeNET; 9130; -.
DR GeneCards; FAM50A; -.
DR HGNC; HGNC:18786; FAM50A.
DR HPA; ENSG00000071859; Low tissue specificity.
DR MalaCards; FAM50A; -.
DR MIM; 300261; phenotype.
DR MIM; 300453; gene.
DR neXtProt; NX_Q14320; -.
DR OpenTargets; ENSG00000071859; -.
DR PharmGKB; PA134984709; -.
DR VEuPathDB; HostDB:ENSG00000071859; -.
DR eggNOG; KOG2894; Eukaryota.
DR GeneTree; ENSGT00390000004735; -.
DR HOGENOM; CLU_037985_1_1_1; -.
DR InParanoid; Q14320; -.
DR OMA; DFIWVFL; -.
DR OrthoDB; 1061864at2759; -.
DR PhylomeDB; Q14320; -.
DR TreeFam; TF314738; -.
DR PathwayCommons; Q14320; -.
DR SignaLink; Q14320; -.
DR BioGRID-ORCS; 9130; 157 hits in 709 CRISPR screens.
DR ChiTaRS; FAM50A; human.
DR GeneWiki; FAM50A; -.
DR GenomeRNAi; 9130; -.
DR Pharos; Q14320; Tbio.
DR PRO; PR:Q14320; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q14320; protein.
DR Bgee; ENSG00000071859; Expressed in sural nerve and 190 other tissues.
DR ExpressionAtlas; Q14320; baseline and differential.
DR Genevisible; Q14320; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0043484; P:regulation of RNA splicing; IMP:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0007283; P:spermatogenesis; NAS:UniProtKB.
DR InterPro; IPR007005; XAP5.
DR PANTHER; PTHR12722; PTHR12722; 1.
DR Pfam; PF04921; XAP5; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Disease variant;
KW Intellectual disability; Isopeptide bond; mRNA processing; mRNA splicing;
KW Nucleus; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..339
FT /note="Protein FAM50A"
FT /id="PRO_0000068284"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 152..155
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 14..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..143
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CROSSLNK 100
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 137
FT /note="A -> V (likely benign variant; it rescues
FT craniofacial patterning defects in zebrafish morphant
FT embryos; dbSNP:rs149558328)"
FT /evidence="ECO:0000269|PubMed:32703943"
FT /id="VAR_084563"
FT VARIANT 143
FT /note="E -> K (likely benign variant; it rescues
FT craniofacial patterning defects in zebrafish morphant
FT embryos; dbSNP:rs782017549)"
FT /evidence="ECO:0000269|PubMed:32703943"
FT /id="VAR_084564"
FT VARIANT 206
FT /note="W -> G (in MRXSA; unknown pathological significance;
FT does not affect FAM50A protein levels in patient cells;
FT does not affect localization to the nucleus)"
FT /evidence="ECO:0000269|PubMed:32703943"
FT /id="VAR_084565"
FT VARIANT 254
FT /note="E -> G (in MRXSA; hypomorphic variant; does not
FT fully rescue craniofacial patterning defects in zebrafish
FT morphant embryos; does not affect FAM50A protein levels in
FT patient cells; does not affect localization to the
FT nucleus)"
FT /evidence="ECO:0000269|PubMed:32703943"
FT /id="VAR_084566"
FT VARIANT 255
FT /note="D -> G (in MRXSA; hypomorphic variant; does not
FT fully rescue craniofacial patterning defects in zebrafish
FT morphant embryos; does not affect localization to the
FT nucleus)"
FT /evidence="ECO:0000269|PubMed:32703943"
FT /id="VAR_084567"
FT VARIANT 255
FT /note="D -> N (in MRXSA; hypomorphic variant; does not
FT fully rescue craniofacial patterning defects in zebrafish
FT morphant embryos)"
FT /evidence="ECO:0000269|PubMed:32703943"
FT /id="VAR_084568"
FT VARIANT 273
FT /note="R -> W (in MRXSA; hypomorphic variant; does not
FT fully rescue craniofacial patterning defects in zebrafish
FT morphant embryos)"
FT /evidence="ECO:0000269|PubMed:32703943"
FT /id="VAR_084569"
FT CONFLICT 166
FT /note="F -> S (in Ref. 2; BAF85808)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="E -> G (in Ref. 2; BAF85808)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 339 AA; 40242 MW; 88BCA57E49B0AA32 CRC64;
MAQYKGAASE AGRAMHLMKK REKQREQMEQ MKQRIAEENI MKSNIDKKFS AHYDAVEAEL
KSSTVGLVTL NDMKAKQEAL VKEREKQLAK KEQSKELQMK LEKLREKERK KEAKRKISSL
SFTLEEEEEG GEEEEEAAMY EEEMEREEIT TKKRKLGKNP DVDTSFLPDR DREEEENRLR
EELRQEWEAK QEKIKSEEIE ITFSYWDGSG HRRTVKMRKG NTMQQFLQKA LEILRKDFSE
LRSAGVEQLM YIKEDLIIPH HHSFYDFIVT KARGKSGPLF NFDVHDDVRL LSDATVEKDE
SHAGKVVLRS WYEKNKHIFP ASRWEPYDPE KKWDKYTIR
